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TNFAIP3-interacting protein 1 (A20-binding inhibitor of NF-kappa-B activation 1) (ABIN-1) (HIV-1 Nef-interacting protein) (Nef-associated factor 1) (Naf1) (Nip40-1) (Virion-associated nuclear shuttling protein) (VAN) (hVAN)

 TNIP1_HUMAN             Reviewed;         636 AA.
Q15025; A4F1W8; A4F1W9; A4F1X2; A4F1X4; A4F1X5; A4F1X6; A4F1X7;
A4F1X9; B7Z699; E7EPY1; E7ET96; O76008; Q05KP3; Q05KP4; Q6N077;
Q96EL9; Q99833; Q9H1J3;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-AUG-1999, sequence version 2.
25-OCT-2017, entry version 166.
RecName: Full=TNFAIP3-interacting protein 1;
AltName: Full=A20-binding inhibitor of NF-kappa-B activation 1;
Short=ABIN-1;
AltName: Full=HIV-1 Nef-interacting protein;
AltName: Full=Nef-associated factor 1;
Short=Naf1;
AltName: Full=Nip40-1;
AltName: Full=Virion-associated nuclear shuttling protein;
Short=VAN;
Short=hVAN;
Name=TNIP1; Synonyms=KIAA0113, NAF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Peripheral blood;
PubMed=9923610; DOI=10.1016/S0014-5793(98)01631-7;
Fukushi M., Dixon J., Kimura T., Tsurutani N., Dixon M.J.,
Yamamoto N.;
"Identification and cloning of a novel cellular protein Naf1, Nef-
associated factor 1, that increases cell surface CD4 expression.";
FEBS Lett. 442:83-88(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Leukocyte;
PubMed=11090181; DOI=10.1128/JVI.74.24.11811-11824.2000;
Gupta K., Ott D., Hope T.J., Siliciano R.F., Boeke J.D.;
"A human nuclear shuttling protein that interacts with human
immunodeficiency virus type 1 matrix is packaged into virions.";
J. Virol. 74:11811-11824(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8),
ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=17016622;
Shiote Y., Ouchida M., Jitsumori Y., Ogama Y., Matsuo Y., Ishimaru F.,
Tanimoto M., Shimizu K.;
"Multiple splicing variants of Naf1/ABIN-1 transcripts and their
alterations in hematopoietic tumors.";
Int. J. Mol. Med. 18:917-923(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[5]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Colon endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 136-636 (ISOFORM 2).
TISSUE=Craniofacial;
PubMed=8681136; DOI=10.1101/gr.6.1.26;
Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.;
"Transcriptional map of the Treacher Collins candidate gene region.";
Genome Res. 6:26-34(1996).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 94-412.
Fukushi M., Kimura T., Yamamoto N.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[13]
FUNCTION, AND INTERACTION WITH MAPK1.
PubMed=12220502; DOI=10.1016/S0006-291X(02)02086-7;
Zhang S., Fukushi M., Hashimoto S., Gao C., Huang L., Fukuyo Y.,
Nakajima T., Amagasa T., Enomoto S., Koike K., Miura O., Yamamoto N.,
Tsuchida N.;
"A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear
signaling.";
Biochem. Biophys. Res. Commun. 297:17-23(2002).
[14]
FUNCTION, AND INTERACTION WITH IKBKG AND TNFAIP3.
PubMed=16684768; DOI=10.1074/jbc.M601502200;
Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A.,
Acquaviva R., Formisano S., Vito P., Leonardi A.;
"ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting
NF-kappaB.";
J. Biol. Chem. 281:18482-18488(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
FUNCTION, INTERACTION WITH SELPLG AND PIK3CD, PHOSPHORYLATION AT
TYR-552, AND MUTAGENESIS OF TYR-552.
PubMed=17632516; DOI=10.1038/ni1491;
Wang H.B., Wang J.T., Zhang L., Geng Z.H., Xu W.L., Xu T., Huo Y.,
Zhu X., Plow E.F., Chen M., Geng J.G.;
"P-selectin primes leukocyte integrin activation during
inflammation.";
Nat. Immunol. 8:882-892(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
FUNCTION, INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, AND MUTAGENESIS
OF 476-GLU-ARG-477.
PubMed=20010814; DOI=10.1038/ncb2006;
Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.;
"A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to
dampen the host NF-kappaB-mediated inflammatory response.";
Nat. Cell Biol. 12:66-73(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-442, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
UBIQUITIN-BINDING, AND MUTAGENESIS OF ASP-472.
PubMed=21606507; DOI=10.1084/jem.20102177;
Nanda S.K., Venigalla R.K., Ordureau A., Patterson-Kane J.C.,
Powell D.W., Toth R., Arthur J.S., Cohen P.;
"Polyubiquitin binding to ABIN1 is required to prevent autoimmunity.";
J. Exp. Med. 208:1215-1228(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-627, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-284, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-599, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[27]
VARIANTS TRP-263; MET-286; THR-374 AND LYS-476.
PubMed=21266526; DOI=10.1158/1078-0432.CCR-10-1859;
Dong G., Chanudet E., Zeng N., Appert A., Chen Y.W., Au W.Y.,
Hamoudi R.A., Watkins A.J., Ye H., Liu H., Gao Z., Chuang S.S.,
Srivastava G., Du M.Q.;
"A20, ABIN-1/2, and CARD11 mutations and their prognostic value in
gastrointestinal diffuse large B-cell lymphoma.";
Clin. Cancer Res. 17:1440-1451(2011).
-!- FUNCTION: Inhibits NF-kappa-B activation and TNF-induced NF-kappa-
B-dependent gene expression by regulating A20/TNFAIP3-mediated
deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to
ubiquitinated IKBKG. Involved in regulation of EGF-induced
ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear
translocation and MAPK1-dependent transcription. Increases cell
surface CD4(T4) antigen expression. Involved in the anti-
inflammatory response of macrophages and positively regulates TLR-
induced activation of CEBPB. Involved in the prevention of
autoimmunity; this function implicates binding to polyubiquitin.
Involved in leukocyte integrin activation during inflammation;
this function is mediated by association with SELPLG and dependent
on phosphorylation by SRC-family kinases. Interacts with HIV-1
matrix protein and is packaged into virions and overexpression can
inhibit viral replication. May regulate matrix nuclear
localization, both nuclear import of PIC (Preintegration complex)
and export of GAG polyprotein and viral genomic RNA during virion
production. In case of infection, promotes association of IKBKG
with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which
in turn promotes polyubiquitination of IKBKG leading to its
proteasome-dependent degradation and thus is perturbing NF-kappa-B
activation during bacterial infection.
{ECO:0000269|PubMed:12220502, ECO:0000269|PubMed:16684768,
ECO:0000269|PubMed:17016622, ECO:0000269|PubMed:17632516,
ECO:0000269|PubMed:20010814}.
-!- SUBUNIT: Interacts with TNFAIP3 and IKBKG (polyubiquitinated);
facilitates TNFAIP3-mediated de-ubiquitination of NEMO/IKBKG.
Interacts with polyubiquitin. Interacts with MAPK1, SELPLG and
PIK3CD. Interacts with IRAK1 (polyubiquitinated). Interacts with
MYD88; the interaction is indicative for participation in an
activated TLR-signaling complex. Interacts with HIV-1 matrix
protein. Interacts with Shigella flexneri ipah9.8; the interaction
promotes polyubiquitination of IKBKG.
{ECO:0000269|PubMed:12220502, ECO:0000269|PubMed:16684768,
ECO:0000269|PubMed:17632516, ECO:0000269|PubMed:20010814}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-357849, EBI-357849;
Q9BXS5:AP1M1; NbExp=3; IntAct=EBI-357849, EBI-541426;
Q13895:BYSL; NbExp=7; IntAct=EBI-357849, EBI-358049;
Q8NEF3:CCDC112; NbExp=3; IntAct=EBI-357849, EBI-745040;
P51959:CCNG1; NbExp=7; IntAct=EBI-357849, EBI-3905829;
Q9H305:CDIP1; NbExp=4; IntAct=EBI-357849, EBI-2876678;
Q96M91:CFAP53; NbExp=3; IntAct=EBI-357849, EBI-742422;
A8MQ03:CYSRT1; NbExp=4; IntAct=EBI-357849, EBI-3867333;
Q08426:EHHADH; NbExp=3; IntAct=EBI-357849, EBI-2339219;
Q3B820:FAM161A; NbExp=5; IntAct=EBI-357849, EBI-719941;
Q92567:FAM168A; NbExp=3; IntAct=EBI-357849, EBI-7957930;
Q9H0R8:GABARAPL1; NbExp=5; IntAct=EBI-357849, EBI-746969;
P60520:GABARAPL2; NbExp=5; IntAct=EBI-357849, EBI-720116;
Q14161:GIT2; NbExp=3; IntAct=EBI-357849, EBI-1046878;
Q00403:GTF2B; NbExp=5; IntAct=EBI-357849, EBI-389564;
Q8N4P3:HDDC3; NbExp=3; IntAct=EBI-357849, EBI-750003;
Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-357849, EBI-81279;
Q8VSC3:ipaH9.8 (xeno); NbExp=4; IntAct=EBI-357849, EBI-6125799;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-357849, EBI-2125614;
Q96M61:MAGEB18; NbExp=5; IntAct=EBI-357849, EBI-741835;
Q9H213:MAGEH1; NbExp=3; IntAct=EBI-357849, EBI-473834;
Q9H492:MAP1LC3A; NbExp=5; IntAct=EBI-357849, EBI-720768;
Q9GZQ8:MAP1LC3B; NbExp=3; IntAct=EBI-357849, EBI-373144;
Q7L9L4:MOB1B; NbExp=3; IntAct=EBI-357849, EBI-2558745;
Q70IA8:MOB3C; NbExp=3; IntAct=EBI-357849, EBI-9679267;
Q9UBU8:MORF4L1; NbExp=3; IntAct=EBI-357849, EBI-399246;
Q15014:MORF4L2; NbExp=3; IntAct=EBI-357849, EBI-399257;
O14777:NDC80; NbExp=5; IntAct=EBI-357849, EBI-715849;
P19838:NFKB1; NbExp=4; IntAct=EBI-357849, EBI-300010;
Q9BYG3:NIFK; NbExp=3; IntAct=EBI-357849, EBI-2561019;
Q9Y5B8:NME7; NbExp=7; IntAct=EBI-357849, EBI-744782;
Q96CV9:OPTN; NbExp=12; IntAct=EBI-357849, EBI-748974;
Q13526:PIN1; NbExp=6; IntAct=EBI-357849, EBI-714158;
Q96T60:PNKP; NbExp=5; IntAct=EBI-357849, EBI-1045072;
Q15311:RALBP1; NbExp=3; IntAct=EBI-357849, EBI-749285;
Q8TAD8:SNIP1; NbExp=3; IntAct=EBI-357849, EBI-749336;
Q5T7P8-2:SYT6; NbExp=3; IntAct=EBI-357849, EBI-10246152;
Q86VP1:TAX1BP1; NbExp=5; IntAct=EBI-357849, EBI-529518;
Q15560:TCEA2; NbExp=6; IntAct=EBI-357849, EBI-710310;
Q96MN5:TCEANC2; NbExp=3; IntAct=EBI-357849, EBI-5462748;
P21580:TNFAIP3; NbExp=6; IntAct=EBI-357849, EBI-527670;
Q96KP6:TNIP3; NbExp=5; IntAct=EBI-357849, EBI-2509913;
P40222:TXLNA; NbExp=5; IntAct=EBI-357849, EBI-359793;
Q9H267:VPS33B; NbExp=5; IntAct=EBI-357849, EBI-749072;
P24278:ZBTB25; NbExp=5; IntAct=EBI-357849, EBI-739899;
O43257:ZNHIT1; NbExp=3; IntAct=EBI-357849, EBI-347522;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
the nucleus and cytoplasm in a CRM1-dependent manner.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Alpha, FL;
IsoId=Q15025-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q15025-2; Sequence=VSP_003913;
Name=3;
IsoId=Q15025-3; Sequence=VSP_045296;
Name=4; Synonyms=Alpha2;
IsoId=Q15025-4; Sequence=VSP_055208;
Name=5; Synonyms=Alpha4;
IsoId=Q15025-5; Sequence=VSP_055209, VSP_055214;
Note=Less effective in the NF-kappa-B inhibitory effect.;
Name=6; Synonyms=Beta2;
IsoId=Q15025-6; Sequence=VSP_055208, VSP_003913;
Name=7; Synonyms=Alpha3, Beta3;
IsoId=Q15025-7; Sequence=VSP_055211, VSP_055212;
Name=8; Synonyms=Beta4;
IsoId=Q15025-8; Sequence=VSP_055210, VSP_055213;
-!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in peripheral
blood lymphocytes, spleen and skeletal muscle, and is weakly
expressed in the brain. In peripheral blood mononucleocytes,
isoform 4 is mainly expressed and isoform 1 and isoform 7 are
almost not expressed. Expression of isoform 1 and isoform 7
increases in leukemic cells. {ECO:0000269|PubMed:17016622}.
-!- PTM: Phosphorylation at Tyr-552 by SRC-family kinases recruits
phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which
results in integrin activation and leukocyte adhesion to activated
endothelium during inflammation. {ECO:0000269|PubMed:17632516}.
-!- SEQUENCE CAUTION:
Sequence=AAB41438.1; Type=Frameshift; Positions=152, 154; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ011895; CAA09855.1; -; mRNA.
EMBL; AJ011896; CAA09856.1; -; mRNA.
EMBL; AY012155; AAG42154.1; -; mRNA.
EMBL; AB177543; BAF34946.1; -; mRNA.
EMBL; AB177544; BAF34947.1; -; mRNA.
EMBL; AB252970; BAF48787.1; -; mRNA.
EMBL; AB252971; BAF48788.1; -; mRNA.
EMBL; AB252972; BAF48789.1; -; mRNA.
EMBL; AB252973; BAF48790.1; -; mRNA.
EMBL; AB252974; BAF48791.1; -; mRNA.
EMBL; AB252975; BAF48792.1; -; mRNA.
EMBL; AB252976; BAF48793.1; -; mRNA.
EMBL; AB252977; BAF48794.1; -; mRNA.
EMBL; AB252978; BAF48795.1; -; mRNA.
EMBL; AB252979; BAF48796.1; -; mRNA.
EMBL; AB252980; BAF48797.1; -; mRNA.
EMBL; AB252981; BAF48798.1; -; mRNA.
EMBL; D30755; BAA06416.2; -; mRNA.
EMBL; AK299975; BAH13185.1; -; mRNA.
EMBL; BX640647; CAE45793.1; -; mRNA.
EMBL; AC008641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61688.1; -; Genomic_DNA.
EMBL; CH471062; EAW61689.1; -; Genomic_DNA.
EMBL; CH471062; EAW61690.1; -; Genomic_DNA.
EMBL; CH471062; EAW61691.1; -; Genomic_DNA.
EMBL; BC012133; AAH12133.1; -; mRNA.
EMBL; BC014008; AAH14008.1; -; mRNA.
EMBL; U39403; AAC99999.1; -; mRNA.
EMBL; U83844; AAB41438.1; ALT_FRAME; mRNA.
CCDS; CCDS34280.1; -. [Q15025-1]
CCDS; CCDS58982.1; -. [Q15025-3]
CCDS; CCDS58983.1; -. [Q15025-5]
CCDS; CCDS58984.1; -. [Q15025-4]
CCDS; CCDS58985.1; -. [Q15025-2]
RefSeq; NP_001239314.1; NM_001252385.1.
RefSeq; NP_001239315.1; NM_001252386.1. [Q15025-3]
RefSeq; NP_001239319.1; NM_001252390.1. [Q15025-1]
RefSeq; NP_001239320.1; NM_001252391.1. [Q15025-1]
RefSeq; NP_001239321.1; NM_001252392.1. [Q15025-2]
RefSeq; NP_001239322.1; NM_001252393.1. [Q15025-2]
RefSeq; NP_001245383.1; NM_001258454.1. [Q15025-1]
RefSeq; NP_001245384.1; NM_001258455.1. [Q15025-4]
RefSeq; NP_001245385.1; NM_001258456.1. [Q15025-5]
RefSeq; NP_006049.3; NM_006058.4. [Q15025-1]
RefSeq; XP_006714814.1; XM_006714751.1. [Q15025-4]
RefSeq; XP_006714815.1; XM_006714752.2. [Q15025-6]
UniGene; Hs.355141; -.
UniGene; Hs.731557; -.
ProteinModelPortal; Q15025; -.
SMR; Q15025; -.
BioGrid; 115602; 103.
CORUM; Q15025; -.
DIP; DIP-27577N; -.
IntAct; Q15025; 101.
MINT; MINT-200912; -.
STRING; 9606.ENSP00000317891; -.
iPTMnet; Q15025; -.
PhosphoSitePlus; Q15025; -.
BioMuta; TNIP1; -.
DMDM; 20138952; -.
EPD; Q15025; -.
MaxQB; Q15025; -.
PaxDb; Q15025; -.
PeptideAtlas; Q15025; -.
PRIDE; Q15025; -.
DNASU; 10318; -.
Ensembl; ENST00000315050; ENSP00000317891; ENSG00000145901. [Q15025-1]
Ensembl; ENST00000518977; ENSP00000430971; ENSG00000145901. [Q15025-2]
Ensembl; ENST00000520931; ENSP00000429891; ENSG00000145901. [Q15025-3]
Ensembl; ENST00000521591; ENSP00000430760; ENSG00000145901. [Q15025-1]
Ensembl; ENST00000522226; ENSP00000428187; ENSG00000145901. [Q15025-1]
Ensembl; ENST00000523200; ENSP00000431105; ENSG00000145901. [Q15025-4]
Ensembl; ENST00000523338; ENSP00000428243; ENSG00000145901. [Q15025-2]
Ensembl; ENST00000524280; ENSP00000429912; ENSG00000145901. [Q15025-5]
Ensembl; ENST00000610535; ENSP00000483944; ENSG00000145901. [Q15025-4]
Ensembl; ENST00000610874; ENSP00000484665; ENSG00000145901. [Q15025-5]
GeneID; 10318; -.
KEGG; hsa:10318; -.
UCSC; uc003ltg.5; human. [Q15025-1]
CTD; 10318; -.
DisGeNET; 10318; -.
EuPathDB; HostDB:ENSG00000145901.14; -.
GeneCards; TNIP1; -.
HGNC; HGNC:16903; TNIP1.
HPA; HPA037893; -.
HPA; HPA037894; -.
HPA; HPA071950; -.
MIM; 607714; gene.
neXtProt; NX_Q15025; -.
OpenTargets; ENSG00000145901; -.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA128394573; -.
eggNOG; ENOG410IEGE; Eukaryota.
eggNOG; ENOG411180D; LUCA.
GeneTree; ENSGT00510000046908; -.
HOGENOM; HOG000253048; -.
HOVERGEN; HBG019072; -.
InParanoid; Q15025; -.
OMA; MQGIKML; -.
OrthoDB; EOG091G04AX; -.
PhylomeDB; Q15025; -.
TreeFam; TF351138; -.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
ChiTaRS; TNIP1; human.
GeneWiki; TNIP1; -.
GenomeRNAi; 10318; -.
PRO; PR:Q15025; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145901; -.
CleanEx; HS_NAF1; -.
CleanEx; HS_TNIP1; -.
ExpressionAtlas; Q15025; baseline and differential.
Genevisible; Q15025; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005622; C:intracellular; TAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:UniProtKB.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0006952; P:defense response; TAS:ProtInc.
GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:UniProtKB.
GO; GO:0085032; P:modulation by symbiont of host I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; TAS:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:1903003; P:positive regulation of protein deubiquitination; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006412; P:translation; TAS:ProtInc.
InterPro; IPR033372; TNIP1.
PANTHER; PTHR31882:SF3; PTHR31882:SF3; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Inflammatory response; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 636 TNFAIP3-interacting protein 1.
/FTId=PRO_0000096691.
REGION 94 412 Interaction with Nef.
REGION 351 367 Interaction with Shigella flexneri
ipah9.8.
REGION 431 588 Required for inhibitory activity of TNF-
induced NF-kappa-B activation.
{ECO:0000250}.
REGION 452 510 Ubiquitin-binding domain (UBD).
COILED 20 73 {ECO:0000255}.
COILED 196 258 {ECO:0000255}.
COILED 294 535 {ECO:0000255}.
MOTIF 524 530 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 539 636 Pro-rich.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 438 438 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 552 552 Phosphotyrosine.
{ECO:0000269|PubMed:17632516}.
MOD_RES 571 571 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9WUU8}.
MOD_RES 599 599 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 599 599 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 627 627 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 53 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17016622,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_045296.
VAR_SEQ 530 593 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:17016622}.
/FTId=VSP_055208.
VAR_SEQ 530 556 ASGERYHVEPHPEHLCGAYPYAYPPMP -> SLQKMTVRGL
SETRLCHLAPPSSCRAS (in isoform 5).
{ECO:0000303|PubMed:17016622}.
/FTId=VSP_055209.
VAR_SEQ 530 552 ASGERYHVEPHPEHLCGAYPYAY -> SQLISDCQETRSHL
HGVARASAG (in isoform 8).
{ECO:0000303|PubMed:17016622}.
/FTId=VSP_055210.
VAR_SEQ 530 545 ASGERYHVEPHPEHLC -> GTHRGCPRRLPERKVK (in
isoform 7).
{ECO:0000303|PubMed:17016622}.
/FTId=VSP_055211.
VAR_SEQ 546 636 Missing (in isoform 7).
{ECO:0000303|PubMed:17016622}.
/FTId=VSP_055212.
VAR_SEQ 553 636 Missing (in isoform 8).
{ECO:0000303|PubMed:17016622}.
/FTId=VSP_055213.
VAR_SEQ 557 636 Missing (in isoform 5).
{ECO:0000303|PubMed:17016622}.
/FTId=VSP_055214.
VAR_SEQ 627 636 SPKNDREGPQ -> PADLRLPRN (in isoform 2 and
isoform 6). {ECO:0000303|PubMed:17016622,
ECO:0000303|PubMed:8681136,
ECO:0000303|PubMed:9923610}.
/FTId=VSP_003913.
VARIANT 103 103 P -> S (in dbSNP:rs2303018).
/FTId=VAR_051453.
VARIANT 146 146 A -> V (in dbSNP:rs2233289).
/FTId=VAR_051454.
VARIANT 151 151 P -> A (in dbSNP:rs2233290).
/FTId=VAR_051455.
VARIANT 233 233 R -> Q (in dbSNP:rs2233292).
/FTId=VAR_051456.
VARIANT 260 260 A -> V (in dbSNP:rs2233295).
/FTId=VAR_051457.
VARIANT 263 263 R -> W (in patients with gastrointestinal
diffuse large cell lymphoma;
dbSNP:rs117663772).
{ECO:0000269|PubMed:21266526}.
/FTId=VAR_067965.
VARIANT 286 286 T -> M (in patients with gastrointestinal
diffuse large cell lymphoma; somatic
mutation; dbSNP:rs185683917).
{ECO:0000269|PubMed:21266526}.
/FTId=VAR_067966.
VARIANT 374 374 I -> T (in patients with gastrointestinal
diffuse large cell lymphoma;
dbSNP:rs748495842).
{ECO:0000269|PubMed:21266526}.
/FTId=VAR_067967.
VARIANT 476 476 E -> K (in patients with gastrointestinal
diffuse large cell lymphoma; somatic
mutation; loss of inhibitory activity on
CARD11- and TNF-induced NF-kappa-B
activation).
{ECO:0000269|PubMed:21266526}.
/FTId=VAR_067968.
MUTAGEN 472 472 D->N: Abolishes binding to polyubiquitin
('K-63'-linked and linear).
{ECO:0000269|PubMed:21606507}.
MUTAGEN 552 552 Y->F: Abolishes interaction with PI3K p85
regulatory subunit and abolishes
interaction between SELPLG and PI3K p85
regulatory subunit.
{ECO:0000269|PubMed:17632516}.
CONFLICT 148 148 G -> D (in Ref. 10; AAH12133).
{ECO:0000305}.
CONFLICT 178 178 G -> S (in Ref. 6; BAH13185).
{ECO:0000305}.
CONFLICT 299 299 A -> P (in Ref. 2; AAG42154 and 3;
BAF34946). {ECO:0000305}.
SEQUENCE 636 AA; 71864 MW; D81B96BEAD50D871 CRC64;
MEGRGPYRIY DPGGSVPSGE ASAAFERLVK ENSRLKEKMQ GIKMLGELLE ESQMEATRLR
QKAEELVKDN ELLPPPSPSL GSFDPLAELT GKDSNVTASP TAPACPSDKP APVQKPPSSG
TSSEFEVVTP EEQNSPESSS HANAMALGPL PREDGNLMLH LQRLETTLSV CAEEPDHGQL
FTHLGRMALE FNRLASKVHK NEQRTSILQT LCEQLRKENE ALKAKLDKGL EQRDQAAERL
REENLELKKL LMSNGNKEGA SGRPGSPKME GTGKKAVAGQ QQASVTAGKV PEVVALGAAE
KKVKMLEQQR SELLEVNKQW DQHFRSMKQQ YEQKITELRQ KLADLQKQVT DLEAEREQKQ
RDFDRKLLLA KSKIEMEETD KEQLTAEAKE LRQKVKYLQD QLSPLTRQRE YQEKEIQRLN
KALEEALSIQ TPPSSPPTAF GSPEGAGALL RKQELVTQNE LLKQQVKIFE EDFQRERSDR
ERMNEEKEEL KKQVEKLQAQ VTLSNAQLKA FKDEEKAREA LRQQKRKAKA SGERYHVEPH
PEHLCGAYPY AYPPMPAMVP HHGFEDWSQI RYPPPPMAME HPPPLPNSRL FHLPEYTWRL
PCGGVRNPNQ SSQVMDPPTA RPTEPESPKN DREGPQ


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